奥美沙坦酯与胰蛋白酶相互作用关系的研究  

Study on Interaction between Olmesartan Medoxomil and Trypsin

作　　者：陈晓春 朱超 付飞娥 陈玲 CHEN Xiaochun;ZHU Chao;FU Feie;CHEN Ling(Yunnan Open University/Yunnan National Defense Industry Vocational and Technical College,Yunnan Kunming 650000,China)

机构地区：[1]云南开放大学/云南国防工业职业技术学院,云南昆明650000

出　　处：《广州化工》2025年第3期26-29,49,共5页GuangZhou Chemical Industry

基　　金：云南省教育厅科学研究基金项目(No:2020J0491)。

摘　　要：采用荧光光谱、紫外光谱等光谱学方法和分子对接模拟法研究了奥美沙坦酯与胰蛋白酶的相互作用机制。结果表明,奥美沙坦酯以静态淬灭的方式使胰蛋白酶的荧光淬灭,奥美沙坦酯与胰蛋白酶以1∶1的形式结合,结合力主要为静电作用力。奥美沙坦酯与胰蛋白酶的结合导致了胰蛋白酶构象的改变。酶活性试验表明,奥美沙坦酯存在轻度减弱了胰蛋白酶活性。分子对接结果显示,相互作用的区域位于胰蛋白酶催化中心,总共有11个氨基酸残基参与了结合。The interaction between olmesartan medoxomil and trypsin was comprehensively examined using fluorescence spectroscopy,ultraviolet spectroscopy and molecular docking simulations.The results indicated that olmesartan medoxomil quenched the fluorescence of trypsin through static quenching.Furthermore,olmesartan medoxomil bound to trypsin in a 1∶1 stoichiometric ratio spontaneously,with the binding force being primarily electrostatic.This binding interaction led to a conformational change in trypsin.Enzyme activity assays revealed a slight reduction in trypsin activity in the presence of olmesartan medoxomil.Molecular docking simulations indicated that the region of interaction was located within the catalytic center of trypsin,involving a total of 11 amino acid residues in the binding process.

关 键 词：奥美沙坦酯 胰蛋白酶 相互作用 分子对接 

分 类 号：Q518.1[生物学—生物化学]